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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제31권 제1호
- 발행연도
- 2021.1
- 수록면
- 79 - 91 (13page)
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γ-Glutamylcysteine synthetase (Gcs1) and glutathione reductase (Glr1) activity maintains minimal levels of cellular methylglyoxal in Candida albicans. In glutathione-depleted Δgcs1, we previously saw that NAD(H)-linked methylglyoxal oxidoreductase (Mgd1) and alcohol dehydrogenase (Adh1) are the most active methylglyoxal scavengers. With methylglyoxal accumulation, disruptants lacking MGD1 or ADH1 exhibit a poor redox state. However, there is little convincing evidence for a reciprocal relationship between methylglyoxal scavenger genes-disrupted mutants and changes in glutathione-(in)dependent redox regulation. Herein, we attempt to demonstrate a functional role for methylglyoxal scavengers, modeled on a triple disruptant (Δmgd1/Δadh1/Δgcs1), to link between antioxidative enzyme activities and their metabolites in glutathione-depleted conditions. Despite seeing elevated methylglyoxal in all of the disruptants, the result saw a decrease in pyruvate content in Δmgd1/Δadh1/Δgcs1 which was not observed in double gene-disrupted strains such as Δmgd1/Δgcs1 and Δadh1/Δgcs1. Interestingly, Δmgd1/Δadh1/Δgcs1 exhibited a significantly decrease in H2O2 and superoxide which was also unobserved in Δmgd1/Δgcs1 and Δadh1/Δgcs1. The activities of the antioxidative enzymes erythroascorbate peroxidase and cytochrome c peroxidase were noticeably higher in Δmgd1/Δadh1/Δgcs1 than in the other disruptants. Meanwhile, Glr1 activity severely diminished in Δmgd1/Δadh1/Δgcs1. Monitoring complementary gene transcripts between double gene-disrupted Δmgd1/Δgcs1 and Δadh1/Δgcs1 supported the concept of an unbalanced redox state independent of the Glr1 activity for Δmgd1/Δadh1/Δgcs1. Our data demonstrate the reciprocal use of Eapx1 and Ccp1 in the absence of both methylglyoxal scavengers; that being pivotal for viability in non-filamentous budding yeast.
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참고문헌 (66)
참고문헌 신청
Ramasamy R / 2012 / Advanced glycation endproducts : from precursors to RAGE : round and round we go / Amino Acids 42:1151~1161
Szent-Györgyi A / 1967 / Keto-aldehydes and cell division / Science 155:539~541
Lee C / 1998 / Oxidation-reduction properties of methylglyoxal-modified protein in relation to free radical generation / J. Biol. Chem 273:25272~25278
Szent-Györgyi A / 1975 / Interaction of glyoxal and methylglyoxal with biogenic amines / Proc. Natl. Acad. Sci. USA 72:1610~1611
Yim H-S / 1995 / Free radicals generated during the glycation reaction of amino acids by methylglyoxal. A model study of protein-cross-linked free radicals / J. Biol. Chem 270:28228~28233
Szent-Györgyi A / 1967 / Keto-aldehydes and cell division / Science 155:539~541
Lee C / 1998 / Oxidation-reduction properties of methylglyoxal-modified protein in relation to free radical generation / J. Biol. Chem 273:25272~25278
Szent-Györgyi A / 1975 / Interaction of glyoxal and methylglyoxal with biogenic amines / Proc. Natl. Acad. Sci. USA 72:1610~1611
Yim H-S / 1995 / Free radicals generated during the glycation reaction of amino acids by methylglyoxal. A model study of protein-cross-linked free radicals / J. Biol. Chem 270:28228~28233
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